Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Uttamkumar Samanta"'
Autor:
Uttamkumar Samanta, Manal A. Swairjo, Jonathan Alvarez, Dirk Iwata-Reuyl, Adriana Bon Ramos, Xianghan Mei
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 85:103-116
The tunneling-fold (T-fold) structural superfamily has emerged as a versatile protein scaffold of diverse catalytic activities. This is especially evident in the pathways to the 7-deazaguanosine modified nucleosides of tRNA queuosine and archaeosine.
Autor:
Brian J. Bahnson, Prabhavathi Srinivasan, Uttamkumar Samanta, Stephen D. Kirby, Douglas M. Cerasoli
Publikováno v:
Biochemical Pharmacology. 78:420-429
The enzyme group-VIIA phospholipase A2 (gVIIA-PLA2) is bound to lipoproteins in human blood and hydrolyzes the ester bond at the sn-2 position of phospholipid substrates with a short sn-2 chain. The enzyme belongs to a serine hydrolase superfamily of
Publikováno v:
Biochemistry. 48:3425-3435
Insecticide and nerve agent organophosphorus (OP) compounds are potent inhibitors of the serine hydrolase superfamily of enzymes. Nerve agents, such as sarin, soman, tabun, and VX exert their toxicity by inhibiting human acetycholinesterase at nerve
Publikováno v:
Protein & Peptide Letters. 16:97-100
The plasma form of the human enzyme platelet activating factor acetylhydrolase (PAF-AH) has been crystallized, and X-ray diffraction data were collected at a synchrotron source to a resolution of 1.47 A. The crystals belong to space group C2, with un
Autor:
Brian J. Bahnson, Uttamkumar Samanta
Publikováno v:
Journal of Biological Chemistry. 283:31617-31624
Human plasma platelet-activating factor (PAF) acetylhydrolase functions by reducing PAF levels as a general anti-inflammatory scavenger and is linked to anaphylactic shock, asthma, and allergic reactions. The enzyme has also been implicated in hydrol
Autor:
Kana M. Sureshan, Mysore S. Shashidhar, Thoniyot Praveen, Uttamkumar Samanta, Pinak Chakrabarti, Tanya Das, Debnath Pal
Publikováno v:
Journal of the Chemical Society, Perkin Transactions 2. :358-365
Silver(I) oxide–silver halide mediated alcoholyses of racemic 2,4-di-O-benzoyl-myo-inositol 1,3,5-orthoformate, and its 6-O-methyl and 6-O-sulfonylated derivatives, under identical conditions have been compared. While only the 4-O-benzoyl group und
Autor:
Xianghan Mei, Jonathan Alvarez, Adriana Bon Ramos, Uttamkumar Samanta, Dirk Iwata-Reuyl, Manal A. Swairjo
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 85:C1-C1
Autor:
Vedavati G. Puranik, Debasis Hazra, Amitabha Sarkar, Mohan M. Bhadbhade, K. N. Jayaprakash, Karl S. Hagen, Uttamkumar Samanta
Publikováno v:
Journal of Organometallic Chemistry. :709-722
Crystallography and proton NMR spectroscopy were used to compare the conformations of aryl amino Fischer carbene complexes with structurally analogous aryl carboxamides. The similarity disappears when the aromatic rings were complexed with tricarbony
Autor:
Uttamkumar Samanta, Pinak Chakrabarti
Publikováno v:
Protein Engineering, Design and Selection. 14:7-15
Instead of looking at the interfacial area as a measure of the extent of a protein--protein recognition site, a new procedure has been developed to identify the importance of a specific residue, namely tryptophan, in the binding process. Trp residues
Publikováno v:
Proteins: Structure, Function, and Genetics. 38:288-300
Although relatively rare, the tryptophan residue (Trp), with its large hydrophobic surface, has a unique role in the folded structure and the binding site of many proteins, and its fluorescence properties make it very useful in studying the structure